Azotobacter Vinelandii Ferredoxin I: Mutagenesis and Reduction Potential Data

Experimental data characterizes Azotobacter vinelandii ferredoxin I variants created to test the contribution of individual amino acid residues to the [4Fe-4S] cluster reduction potential. The dataset includes results from x-ray crystallography, absorption, CD, EPR, and 1H NMR spectroscopies, and electrochemical methods. The work was authored by C.D. Stout from the University of California, Irvine.

Use Cases

• Modeling the relationship between protein surface charge and reduction potential based on mutagenesis data.
• Analyzing spectroscopic signatures of [4Fe-4S] clusters based on absorption, CD, EPR, and NMR data.
• Training models to predict protein structural stability from x-ray crystallography results of mutated residues.
• Comparing reduction potential differences between homologous proteins based on solvent accessibility.

Strengths

• Data includes results from multiple characterization methods: x-ray crystallography, absorption, CD, EPR, 1H NMR, and electrochemistry.
• Study tests a specific hypothesis by converting residues in AvFdI into corresponding residues from a homologous protein (PaFd).
• Analysis includes six distinct mutations involving both surface-charged and buried hydrophobic residues.

Limitations

• Row count and dataset scale are unknown, which may limit suitability assessment.
• Column-level documentation is absent; field semantics must be inferred after download.
• Last update date is unknown; freshness unverified.

Provenance

Source

University of California, Irvine (author C.D. Stout), via paperswithcode.

Collection Method

Experimental study involving site-directed mutagenesis, protein characterization, and electrochemical analysis.